Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
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- 4 August 2006
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 313 (5787) , 670-673
- https://doi.org/10.1126/science.1129594
Abstract
Immunoglobulin G (IgG) mediates pro- and anti-inflammatory activities through the engagement of its Fc fragment (Fc) with distinct Fcg receptors (FcgRs). One class of Fc-FcgR interactions generates pro-inflammatory effects of immune complexes and cytotoxic antibodies. In contrast, therapeutic intravenous gamma globulin and its Fc fragments are anti-inflammatory. We show here that these distinct properties of the IgG Fc result from differential sialylation of the Fc core polysaccharide. IgG acquires anti-inflammatory properties upon Fc sialylation, which is reduced upon the induction of an antigen-specific immune response. This differential sialylation may provide a switch from innate anti-inflammatory activity in the steady state to generating adaptive pro-inflammatory effects upon antigenic challenge.Keywords
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